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Solution structure of a putative ribosome binding protein from Mycoplasma pneumoniae and comparison to a distant homolog

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Journal of Structural and Functional Genomics

Abstract

The solution structure of MPN156, a ribosome-binding factor A (RBFA) protein family member from Mycoplasma pneumoniae, is presented. The structure, solved by nuclear magnetic resonance, has a type II KH fold typical of RNA binding proteins. Despite only ∼20% sequence identity between MPN156 and another family member from Escherichia coli, the two proteins have high structural similarity. The comparison demonstrates that many of the conserved residues correspond to conserved elements in the structures. Compared to a structure based alignment, standard alignment methods based on sequence alone mispair a majority of amino acids in the two proteins. Implications of these discrepancies for sequence based structural modeling are discussed.

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Authors and Affiliations

  1. Department of Chemistry, University of California, Berkeley, CA, 94720, USA

    Seth M. Rubin & David E. Wemmer

  2. Physical Biosciences Division, Lawrence Berkeley National Laboratory, 1 Cyclotron Rd., Berkeley, CA, 94720, USA

    Seth M. Rubin, Jeffrey G. Pelton, Hisao Yokota, Rosalind Kim & David E. Wemmer

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  1. Seth M. Rubin
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  2. Jeffrey G. Pelton
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Rubin, S.M., Pelton, J.G., Yokota, H. et al. Solution structure of a putative ribosome binding protein from Mycoplasma pneumoniae and comparison to a distant homolog. J Struct Func Genom 4, 235–243 (2003). https://doi.org/10.1023/B:JSFG.0000016127.57320.82

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  • DOI: https://doi.org/10.1023/B:JSFG.0000016127.57320.82

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